D-serine has been known as a compound that is useful as a synthesis intermediate for medicaments such as D-cycloserine.
Hitherto, as an enzyme having activity of synthesizing D-serine from formaldehyde and glycine, only D-threonine aldolase (hereafter to be abbreviated as “DTA”), which is derived from Arthrobacter sp. DK-19, has been known (JP Patent Publication (Kokai) No. 58-116690 A (1983)).
With the use of such DTA, it has been reported that the amount of D-serine produced was 2.5 mmol when 50 mmol each of formaldehyde and glycine were subjected to reaction at 30° C. for 40 hours. (The yield relative to formaldehyde was merely 5%.)
Meanwhile, it has been reported that DTA derived from Arthrobacter sp. DK-38, which is a microorganism of the same genus Arthrobacter, has a broad substrate specificity that responds to D-threonine, D-β-hydroxyphenylserine, D-β-hydroxy-α-aminovaleric acid, and the like; however, it does not react with D-serine (see Eur. J. Biochem., 1997, 248, pp. 385-393).
In addition, it has been reported that D-β-hydroxyamino acids can be produced from glycine and an aldehyde compound with the use of DTA derived from the genus Xanthomonas (JP Patent Publication (Kokai) No. 5-168484 A (1993)). However, it has not been reported that D-serine can be synthesized from formaldehyde and glycine with the use of DTA derived from the genus Xanthomonas. 